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Protein

Inosine-5'-monophosphate dehydrogenase

Gene

impdh

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.UniRule annotation

Catalytic activityi

Inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH.UniRule annotation

Cofactori

K+UniRule annotation

Enzyme regulationi

Mycophenolic acid (MPA) is a non-competitive inhibitor that prevents formation of the closed enzyme conformation by binding to the same site as the amobile flap. In contrast, mizoribine monophosphate (MZP) is a competitive inhibitor that induces the closed conformation. MPA is a potent inhibitor of mammalian IMPDHs but a poor inhibitor of the bacterial enzymes. MZP is a more potent inhibitor of bacterial IMPDH.UniRule annotation

Pathwayi: XMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes XMP from IMP.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Inosine-5'-monophosphate dehydrogenase (impdh)
This subpathway is part of the pathway XMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes XMP from IMP, the pathway XMP biosynthesis via de novo pathway and in Purine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi329Potassium; via carbonyl oxygenUniRule annotation1
Metal bindingi331Potassium; via carbonyl oxygenUniRule annotation1
Binding sitei332IMPUniRule annotation1
Active sitei334Thioimidate intermediateUniRule annotation1
Metal bindingi334Potassium; via carbonyl oxygenUniRule annotation1
Active sitei430Proton acceptorUniRule annotation1
Binding sitei442IMPUniRule annotation1
Metal bindingi501Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1
Metal bindingi502Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi277 – 279NADUniRule annotation3
Nucleotide bindingi327 – 329NADUniRule annotation3

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processGMP biosynthesis, Purine biosynthesis
LigandMetal-binding, NAD, Potassium

Enzyme and pathway databases

ReactomeiR-DDI-6798695 Neutrophil degranulation
R-DDI-73817 Purine ribonucleoside monophosphate biosynthesis
UniPathwayiUPA00601; UER00295

Names & Taxonomyi

Protein namesi
Recommended name:
Inosine-5'-monophosphate dehydrogenaseUniRule annotation (EC:1.1.1.205UniRule annotation)
Short name:
IMP dehydrogenaseUniRule annotation
Short name:
IMPDUniRule annotation
Short name:
IMPDHUniRule annotation
Gene namesi
Name:impdh
Synonyms:guaB
ORF Names:DDB_G0283701
OrganismiDictyostelium discoideum (Slime mold)
Taxonomic identifieri44689 [NCBI]
Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyostelidsDictyostelialesDictyosteliaceaeDictyostelium
Proteomesi
  • UP000002195 Componentsi: Chromosome 4, Unassembled WGS sequence

Organism-specific databases

dictyBaseiDDB_G0283701 guaB

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003281521 – 515Inosine-5'-monophosphate dehydrogenaseAdd BLAST515

Proteomic databases

PaxDbiQ54QQ0
PRIDEiQ54QQ0

Expressioni

Inductioni

Down-regulated by Legionella pneumophila infection.1 Publication

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi44689.DDB0230098

Structurei

3D structure databases

ProteinModelPortaliQ54QQ0
SMRiQ54QQ0
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini120 – 179CBS 1UniRule annotationAdd BLAST60
Domaini183 – 239CBS 2UniRule annotationAdd BLAST57

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni367 – 369IMP bindingUniRule annotation3
Regioni390 – 391IMP bindingUniRule annotation2
Regioni414 – 418IMP bindingUniRule annotation5

Sequence similaritiesi

Belongs to the IMPDH/GMPR family.UniRule annotation

Keywords - Domaini

CBS domain, Repeat

Phylogenomic databases

eggNOGiKOG2550 Eukaryota
COG0516 LUCA
COG0517 LUCA
InParanoidiQ54QQ0
KOiK00088
OMAiGIGIVHK
PhylomeDBiQ54QQ0

Family and domain databases

CDDicd00381 IMPDH, 1 hit
HAMAPiMF_01964 IMPDH, 1 hit
InterProiView protein in InterPro
IPR000644 CBS_dom
IPR005990 IMP_DH
IPR015875 IMP_DH/GMP_Rdtase_CS
IPR001093 IMP_DH_GMPRt
PfamiView protein in Pfam
PF00571 CBS, 2 hits
PF00478 IMPDH, 1 hit
PIRSFiPIRSF000130 IMPDH, 1 hit
SMARTiView protein in SMART
SM00116 CBS, 2 hits
TIGRFAMsiTIGR01302 IMP_dehydrog, 1 hit
PROSITEiView protein in PROSITE
PS51371 CBS, 2 hits
PS00487 IMP_DH_GMP_RED, 1 hit

Sequencei

Sequence statusi: Complete.

Q54QQ0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKINKILQG TNSEYKSEWF VDGFDCFELF QQRHGYTYDD LIMLPGHINF
60 70 80 90 100
SADDVSLKTK LTKNISLNAP LVSSPMDTVT EHLMAINMAL LGGIGIIHYN
110 120 130 140 150
NTVEEQVVEV KKVKRFKNGF ITDPIVLSPT HKLSDVDMIK QKYGFSGIPI
160 170 180 190 200
TDTGRIGGKL VGIVTSRDTD FIKDRSTTLS EVMTTDLITG QQNCTLEEAN
210 220 230 240 250
SILKSCKKGK LPIVNDKGEL VALASRDDLV KNRDFPMATK DHENKKLLVG
260 270 280 290 300
AALGTRETDK ERLAALSDAG VDVVILDSSQ GDSTYQREMI RFIKRNYPKI
310 320 330 340 350
DVIGGNVVTT SQCESLIQAG VDGLRVGMGV GSICTTQEVM ACGRPQATAV
360 370 380 390 400
FKCALYSSQY NVPIIADGGI RTIGHIIKGL SLGASSVMMG SMLAGTEEAP
410 420 430 440 450
GDYFYKDGMR LKKYRGMGSL EAMVKGGDQR YFSETDKIKV AQGVSGSVVD
460 470 480 490 500
KGSVKKFVPY LIQGIKHGLQ DLGCNSVTNL RESVYGGKVR FEVRTAAAQV
510
EGSVHSLFSY EKHFI
Length:515
Mass (Da):56,311
Last modified:May 24, 2005 - v1
Checksum:i054EFBD2EB940868
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAFI02000056 Genomic DNA Translation: EAL65617.1
RefSeqiXP_638973.1, XM_633881.1

Genome annotation databases

EnsemblProtistsiEAL65617; EAL65617; DDB_G0283701
GeneIDi8624219
KEGGiddi:DDB_G0283701

Similar proteinsi

Entry informationi

Entry nameiIMDH_DICDI
AccessioniPrimary (citable) accession number: Q54QQ0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: May 24, 2005
Last modified: May 23, 2018
This is version 96 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

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